SLIDE, the Protein Interacting Domain of Imitation Switch Remodelers, Binds DDT-Domain Proteins of Different Subfamilies in Chromatin Remodeling Complexes

编号 zgly0001461310

文献类型 期刊论文

文献题名 SLIDE, the Protein Interacting Domain of Imitation Switch Remodelers, Binds DDT-Domain Proteins of Different Subfamilies in Chromatin Remodeling Complexes

作者 Jiaqiang Dong  Zheng Gao  Shujing Liu  Guang Li  Zhongnan Yang  Hai Huang  Lin Xu 

作者单位 National Laboratory of Plant Molecular Genetics  Institute of Plant Physiology & Ecology  Shanghai Institutes for Biological Sciences  the Chinese Academy of Sciences  College of Life and Environment Sciences  Shanghai Normal University 

母体文献 Journal of Integrative Plant Biology 

年卷期 2013年10期

年份 2013 

分类号 Q78 

关键词 Arabidopsis  chromatin remodeling factors  DDT-domain proteins  Imitation Switch  protein interaction. 

文摘内容 The Imitation Switch(ISWI)type adenosine triphosphate(ATP)-dependent chromatin remodeling factors are conserved proteins in eukaryotes,and some of them are known to form stable remodeling complexes with members from a family of proteins,termed DDT domain proteins.Although it is well documented that ISWIs play important roles in different biological processes in many eukaryotic species,the molecular basis for protein interactions in ISWI complexes has not been fully addressed.Here,we report the identi cation of interaction domains for both ISWI and DDT domain proteins.By analyzing CHROMATIN REMODELING11(CHR11)and RINGLET1(RLT1),an Arabidopsis thaliana ISWI(AtISWI)and AtDDT domain protein,respectively,we show that the SLIDE domain of CHR11 and the DDT domain together with an adjacent sequence of RLT1 are responsible for their binding.The Arabidopsis genome contains at least 12genes that encode DDT domain proteins,which could be grouped into ve subfamilies based on the sequence similarity.The SLIDE domain of AtISWI is able to bind members from different AtDDT subfamilies.Moreover,a human ISWI protein SNF2H is capable of binding AtDDT domain proteins through its SLIDE domain,suggesting that binding to DDT domain proteins is a conserved biochemical function for the SLIDE domain of ISWIs in eukaryotes.